GenomeNet

Database: UniProt/SWISS-PROT
Entry: PFKAM_MOUSE
LinkDB: PFKAM_MOUSE
Original site: PFKAM_MOUSE 
ID   PFKAM_MOUSE             Reviewed;         780 AA.
AC   P47857; C8CMN5; C8CMN6; C8CMN7; O35513; Q543L1; Q9JK94;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   13-FEB-2019, entry version 179.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=PFK-M;
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=6-phosphofructokinase type A;
DE   AltName: Full=Phosphofructo-1-kinase isozyme A;
DE            Short=PFK-A;
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=Pfkm; Synonyms=Pfk-m, Pfka;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=SWR/J; TISSUE=Brain;
RX   PubMed=11137296; DOI=10.1016/S0378-1119(00)00463-7;
RA   Gunasekera D., Kemp R.G.;
RT   "Genomic organization, 5'flanking region and tissue-specific
RT   expression of mouse phosphofructokinase C gene.";
RL   Gene 260:103-112(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Kidney, Spinal cord, and Thymus {ECO:0000312|EMBL:AK138788};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-213 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [GENOMIC DNA] OF 259-345.
RC   STRAIN=ICR;
RX   PubMed=7980403; DOI=10.1042/bj3030449;
RA   Nakajima H., Noguchi T., Hamaguchi T., Tomita K., Hanafusa T.,
RA   Kono N., Tanaka T., Kuwajima M., Matsuzawa Y.;
RT   "Expression of mouse phosphofructokinase-M gene alternative
RT   transcripts: evidence for the conserved two-promoter system.";
RL   Biochem. J. 303:449-453(1994).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION,
RP   CATALYTIC ACTIVITY, INTERACTION WITH GSTM5 AND HK1, SUBCELLULAR
RP   LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:ACU65459.1};
RX   PubMed=19889946; DOI=10.1095/biolreprod.109.080580;
RA   Nakamura N., Mori C., Eddy E.M.;
RT   "Molecular complex of three testis-specific isozymes associated with
RT   the mouse sperm fibrous sheath: hexokinase 1, phosphofructokinase M,
RT   and glutathione S-transferase mu class 5.";
RL   Biol. Reprod. 82:504-515(2010).
RN   [5]
RP   PROTEIN SEQUENCE OF 367-374, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000269|PubMed:19889946}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03184,
CC         ECO:0000269|PubMed:19889946};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
CC       fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
CC       citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homo- and heterotetramers (By similarity).
CC       Phosphofructokinase (PFK) enzyme functions as a tetramer composed
CC       of different combinations of 3 types of subunits, called PFKM (M),
CC       PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
CC       according to the tissue type it is present in. The kinetic and
CC       regulatory properties of the tetrameric enzyme are dependent on
CC       the subunit composition, hence can vary across tissues (Probable).
CC       Isoform 2 and isoform 3 interact (via N-terminal testis-specific
CC       region) with GSTM5. Isoform 2 and isoform 3 interact (via C-
CC       terminus) with HK1 (via N-terminal spermatogenic cell-specific
CC       region). {ECO:0000255|HAMAP-Rule:MF_03184,
CC       ECO:0000269|PubMed:19889946, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, cilium,
CC       flagellum {ECO:0000269|PubMed:19889946}. Note=Principal piece
CC       region of the sperm flagellum. {ECO:0000269|PubMed:19889946}.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cell projection, cilium,
CC       flagellum {ECO:0000269|PubMed:19889946}. Note=Principal piece
CC       region of the sperm flagellum. {ECO:0000269|PubMed:19889946}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P47857-1; Sequence=Displayed;
CC       Name=2; Synonyms=Pfkms_V4 {ECO:0000303|PubMed:19889946};
CC         IsoId=P47857-2; Sequence=VSP_057079;
CC       Name=3; Synonyms=Pfkms_V3 {ECO:0000303|PubMed:19889946};
CC         IsoId=P47857-3; Sequence=VSP_057080;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle (at
CC       protein level). Isoform 2 and isoform 3 are testis-specific and
CC       are detected in quiescent sperm (at protein level). They are first
CC       detected in the cytoplasm of round spermatids and subsequently in
CC       the flagellum of elongated spermatids extending into the
CC       seminiferous tubule lumen (at protein level). Isoform 2 is
CC       expressed at higher level than isoform 3 in testis.
CC       {ECO:0000269|PubMed:19889946}.
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are first seen on
CC       postnatal day 16 corresponding to the age when midpachytene
CC       spermatocytes are present in the synchronous first wave of
CC       spermatogenesis. Isoform 2 and isoform 3 levels increase
CC       substantially between days 14 and 18 and continue to increase to
CC       age 30 days of neonatal testis development.
CC       {ECO:0000269|PubMed:19889946}.
CC   -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
CC       clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK138788; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305|PubMed:19889946};
DR   EMBL; AF249894; AAF63762.1; -; mRNA.
DR   EMBL; AK002711; BAB22303.1; -; mRNA.
DR   EMBL; AK049773; BAC33913.1; -; mRNA.
DR   EMBL; AK138788; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; D21864; BAA21892.1; -; Genomic_DNA.
DR   EMBL; D21865; BAA21012.1; -; mRNA.
DR   EMBL; GQ428204; ACU65458.1; -; mRNA.
DR   EMBL; GQ428205; ACU65459.1; -; mRNA.
DR   EMBL; GQ428206; ACU65460.1; -; mRNA.
DR   CCDS; CCDS27786.1; -. [P47857-1]
DR   PIR; S53317; S53317.
DR   RefSeq; NP_001156959.1; NM_001163487.1. [P47857-1]
DR   RefSeq; NP_001156960.1; NM_001163488.1. [P47857-1]
DR   RefSeq; NP_067489.3; NM_021514.4. [P47857-1]
DR   RefSeq; XP_006520664.1; XM_006520601.3. [P47857-2]
DR   RefSeq; XP_006520665.1; XM_006520602.2.
DR   UniGene; Mm.272582; -.
DR   UniGene; Mm.384023; -.
DR   ProteinModelPortal; P47857; -.
DR   SMR; P47857; -.
DR   BioGrid; 202125; 2.
DR   ComplexPortal; CPX-2049; 6-phosphofructokinase, M4 homotetramer.
DR   ComplexPortal; CPX-2055; 6-phosphofructokinase, ML3 heterotetramer.
DR   ComplexPortal; CPX-2056; 6-phosphofructokinase, M2L2 heterotetramer.
DR   ComplexPortal; CPX-2057; 6-phosphofructokinase, M3L heterotetramer.
DR   IntAct; P47857; 7.
DR   MINT; P47857; -.
DR   STRING; 10090.ENSMUSP00000059801; -.
DR   iPTMnet; P47857; -.
DR   PhosphoSitePlus; P47857; -.
DR   SwissPalm; P47857; -.
DR   EPD; P47857; -.
DR   jPOST; P47857; -.
DR   MaxQB; P47857; -.
DR   PaxDb; P47857; -.
DR   PeptideAtlas; P47857; -.
DR   PRIDE; P47857; -.
DR   Ensembl; ENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065. [P47857-1]
DR   Ensembl; ENSMUST00000163507; ENSMUSP00000132803; ENSMUSG00000033065. [P47857-1]
DR   Ensembl; ENSMUST00000230445; ENSMUSP00000155809; ENSMUSG00000033065. [P47857-1]
DR   GeneID; 18642; -.
DR   KEGG; mmu:18642; -.
DR   UCSC; uc007xlv.2; mouse. [P47857-1]
DR   CTD; 5213; -.
DR   MGI; MGI:97548; Pfkm.
DR   eggNOG; KOG2440; Eukaryota.
DR   eggNOG; COG0205; LUCA.
DR   GeneTree; ENSGT00940000155440; -.
DR   HOGENOM; HOG000200154; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P47857; -.
DR   KO; K00850; -.
DR   OMA; KQYDELC; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; P47857; -.
DR   TreeFam; TF300411; -.
DR   Reactome; R-MMU-70171; Glycolysis.
DR   SABIO-RK; P47857; -.
DR   UniPathway; UPA00109; UER00182.
DR   ChiTaRS; Pfkm; mouse.
DR   PMAP-CutDB; P47857; -.
DR   PRO; PR:P47857; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000033065; Expressed in 314 organ(s), highest expression level in skeletal muscle tissue.
DR   ExpressionAtlas; P47857; baseline and differential.
DR   Genevisible; P47857; MM.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; ISO:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:MGI.
DR   GO; GO:0016208; F:AMP binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR   GO; GO:0070061; F:fructose binding; ISO:MGI.
DR   GO; GO:0070095; F:fructose-6-phosphate binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0008443; F:phosphofructokinase activity; IDA:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0061621; P:canonical glycolysis; IMP:MGI.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:MGI.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR   GO; GO:0006007; P:glucose catabolic process; IBA:GO_Central.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR   GO; GO:0093001; P:glycolysis from storage polysaccharide through glucose-1-phosphate; IMP:MGI.
DR   GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR   GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IDA:MGI.
DR   GO; GO:0043170; P:macromolecule metabolic process; IC:MGI.
DR   GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051259; P:protein complex oligomerization; ISO:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR   HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Cell projection; Cilium; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Flagellum; Glycolysis; Glycoprotein;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:P00511}.
FT   CHAIN         2    780       ATP-dependent 6-phosphofructokinase,
FT                                muscle type.
FT                                /FTId=PRO_0000112018.
FT   NP_BIND      88     89       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   NP_BIND     118    121       ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   REGION        2    390       N-terminal catalytic PFK domain 1.
FT   REGION      164    166       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      208    210       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      298    301       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      391    401       Interdomain linker.
FT   REGION      402    780       C-terminal regulatory PFK domain 2.
FT   REGION      528    532       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      573    575       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   REGION      661    664       Allosteric activator fructose 2,6-
FT                                bisphosphate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   ACT_SITE    166    166       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   METAL       119    119       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING      25     25       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     201    201       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     264    264       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     292    292       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_03184}.
FT   BINDING     471    471       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     566    566       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     629    629       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     655    655       Allosteric activator fructose 2,6-
FT                                bisphosphate; shared with dimeric
FT                                partner. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   BINDING     735    735       Allosteric activator fructose 2,6-
FT                                bisphosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03184}.
FT   MOD_RES       2      2       N-acetylthreonine.
FT                                {ECO:0000250|UniProtKB:P00511}.
FT   MOD_RES     133    133       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P47858}.
FT   MOD_RES     377    377       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     667    667       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P08237}.
FT   MOD_RES     775    775       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00511}.
FT   CARBOHYD    530    530       O-linked (GlcNAc) serine. {ECO:0000250}.
FT   VAR_SEQ       1      1       M -> MRREEFQLRFFMCVIESRQVVRTTQSTAGEASTSNM
FT                                TIPESKADDQWRLDGMDDDPSTVGPVSIPDTEWIM (in
FT                                isoform 2).
FT                                {ECO:0000269|PubMed:19889946}.
FT                                /FTId=VSP_057079.
FT   VAR_SEQ       1      1       M -> MEEKLTCSFKLLTELLNLITPLAQALFGKRLQNSIL
FT                                DPGDCLSEFTLEERKASGICQPHLFSKHKEINLFLQGILTC
FT                                YEVAMRREEFQLRFFMCVIESRQVVRTTQSTAGEASTSNMT
FT                                IPESKADDQWRLDGMDDDPSTVGPVSIPDTEWIM (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:19889946}.
FT                                /FTId=VSP_057080.
SQ   SEQUENCE   780 AA;  85269 MW;  7917C7AC108B25C7 CRC64;
     MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
     GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
     SLTGADTFRS EWSDLLNDLQ KDGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
     ALHRIVEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
     EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
     RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
     AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL HTVAVMNVGA PAAGMNAAVR
     STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ
     ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI
     GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
     TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
     HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
     QPVTELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
//
DBGET integrated database retrieval system